7VY5

Coxsackievirus B3 (VP3-234Q) incubation with CD55 at pH7.4

7VY5 の概要

• エントリーDOI: 10.2210/pdb7vy5/pdb
• EMDBエントリー: 32194
• 分子名称: Capsid protein VP1, Capsid protein VP2, Capsid protein VP3, ... (6 entities in total)
• 機能のキーワード: cvb3, vp3-234q, cd55, virus
• 由来する生物種: Coxsackievirus B3; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 105613.03

構造登録者

Wang, Q.L.,Liu, C.C. (登録日: 2021-11-13, 公開日: 2022-01-19, 最終更新日: 2024-10-30)

主引用文献

Wang, Q.,Yang, Q.,Liu, C.,Wang, G.,Song, H.,Shang, G.,Peng, R.,Qu, X.,Liu, S.,Cui, Y.,Wang, P.,Xu, W.,Zhao, X.,Qi, J.,Yang, M.,Gao, G.F.
Molecular basis of differential receptor usage for naturally occurring CD55-binding and -nonbinding coxsackievirus B3 strains.
Proc.Natl.Acad.Sci.USA, 119:-, 2022

PubMed Abstract: Receptor usage defines cell tropism and contributes to cell entry and infection. Coxsackievirus B (CVB) engages coxsackievirus and adenovirus receptor (CAR), and selectively utilizes the decay-accelerating factor (DAF; CD55) to infect cells. However, the differential receptor usage mechanism for CVB remains elusive. This study identified VP3-234 residues (234Q/N/V/D/E) as critical population selection determinants during CVB3 virus evolution, contributing to diverse binding affinities to CD55. Cryoelectron microscopy (cryo-EM) structures of CD55-binding/nonbinding isolates and their complexes with CD55 or CAR were obtained under both neutral and acidic conditions, and the molecular mechanism of VP3-234 residues determining CD55 affinity/specificity for naturally occurring CVB3 strains was elucidated. Structural and biochemical studies in vitro revealed the dynamic entry process of CVB3 and the function of the uncoating receptor CAR with different pH preferences. This work provides detailed insight into the molecular mechanism of CVB infection and contributes to an in-depth understanding of enterovirus attachment receptor usage.

PubMed: 35046043
DOI: 10.1073/pnas.2118590119

実験手法

ELECTRON MICROSCOPY (3.15 Å)